| Full text | |
| Author(s): |
Sasaki, Sergio D.
;
Lima, Cássia A. de
;
Lovato, Diogo V.
;
Juliano, Maria A.
;
Torquato, Ricardo J. S.
;
Tanaka, Aparecida S.
[6]
Total Authors: 6
|
| Document type: | Journal article |
| Source: | Experimental Parasitology; v. 118, n. 2, p. 214-220, Feb. 2008. |
| Field of knowledge: | Biological Sciences - Biochemistry |
| Abstract | |
BmSI-7 and BmSI-6, two Boophilus microplus subtilisin inhibitors (BmSI) were purified and characterized from eggs. The inhibitors isolated by classical purification methods presented molecular masses of 7408 and 7271 Da, respectively, by MALDI-TOF-MS. Both BmSI-7 and BmSI-6 inhibited neutrophil elastase (Ki 0.4 and 0.3 nM) and subtilisin A (Ki 1.4 nM for both inhibitors). They also strongly inhibited Pr1 proteases from the fungus Metarhizium anisopliae; BmSI-7 (Ki 50 nM) and BmSI-6 (Ki 2.2 nM). The BmSI-7 full length cDNA was obtained using amino acid sequence information of BmSI-7 peptides generated by proteolytic digestion. BmSI-7 belongs to trypsin inhibitor like cysteine rich domain family (TIL), and it is transcribed in ovary, fat body, gut, salivary gland and haemocytes. BmSI-7 is the first TIL inhibitor described with inhibitory activity toward subtilisin A and Pr1 proteases of entomopathogenic fungi. (AU) | |
| FAPESP's process: | 05/03514-9 - Studies of the physiological function and biotechnological potential of protease inhibitors and anti-hemostatics in hematophagous arthropods |
| Grantee: | Aparecida Sadae Tanaka |
| Support Opportunities: | Research Projects - Thematic Grants |